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TitleCholesterol efflux mechanism revealed by structural analysis of human ABCA1 conformational states.
Journal, issue, pagesNat Cardiovasc Res, Vol. 1, Issue 3, Page 238-245, Year 2022
Publish dateMar 3, 2022
AuthorsYingyuan Sun / Xiaochun Li /
PubMed AbstractATP-binding cassette transporter A1 (ABCA1) utilizes energy derived from ATP hydrolysis to export cholesterol and phospholipids from macrophages. ABCA1 plays a central role in the biosynthesis of ...ATP-binding cassette transporter A1 (ABCA1) utilizes energy derived from ATP hydrolysis to export cholesterol and phospholipids from macrophages. ABCA1 plays a central role in the biosynthesis of high-density lipoprotein (HDL), which mediates reverse cholesterol transport and prevents detrimental lipid deposition. Mutations in ABCA1 cause Tangier disease characterized by a remarkable reduction in the amount of HDL in blood. Here we present cryo-electron microscopy structures of human ABCA1 in ATP-bound and nucleotide-free states. Structural comparison reveals that ATP molecules pull the nucleotide-binding domains together, inducing movements of transmembrane helices 1, 2, 7 and 8 through a series of salt-bridge interactions. Subsequently, extracellular domains (ECDs) undergo a rotation and introduce conformational changes in the ECD-transmembrane interface. In addition, while we observe a sterol-like molecule in ECDs, no such density was observed in the structure of an HDL-deficiency mutant ABCA1, demonstrating the physiological importance of ECDs and a putative interaction mode between ABCA1 and its lipid acceptors. Thus, these structures, along with cholesterol efflux assays, advance the understanding ABCA1-mediated reverse cholesterol transport.
External linksNat Cardiovasc Res / PubMed:37181814 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 4.3 Å
Structure data

25800

7tbw

EMDB-25800, PDB-7tbw:
The structure of ATP-bound ABCA1
Method: EM (single particle) / Resolution: 3.1 Å

25801

7tby

EMDB-25801, PDB-7tby:
The structure of human ABCA1 in nanodisc
Method: EM (single particle) / Resolution: 4.0 Å

25802

7tbz

EMDB-25802, PDB-7tbz:
The structure of ABCA1 Y482C
Method: EM (single particle) / Resolution: 4.3 Å

25803

7tc0

EMDB-25803, PDB-7tc0:
The structure of human ABCA1 in digitonin
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / HDL / cholesterol / Tangier Disease / ABC transporter

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